Raman and near-resonance Raman spectroscopy will be used to probe the conformation of lipids and proteins and the sites of interaction in lipid-protein binding. Preliminary studies have concentrated on assigning and explaining the conformation dependence of lipid polar head group vibrations. These new band assignment greatly extend the amount of information which can be determined, so that now the polar head geometry and bulk lipid packing in addition to side chain geometry can be determined from Raman measurements of lipids. The polar head geometry, packing geometry and side chain geometry of lipids are to be determined as a function of temperature, pH, interactions with metallic cations and state of hydration. These measurements will be made both in the presence and absence of proteins. Also lipid-induced conformation changes in protein will be determined by measurement of backbone-sensitive protein Raman bands in Raman and near-resonance Raman experiments. Preliminary results are presented. To begin with a very general model for which x-ray diffraction and esr spectroscopy results are available for comparison, we have chosen to study in the lipid-protein interaction studies the interaction of lysozyme with specific lipids. Varying the pH will serve to change the type of lipid-protein interactions so that models of electrostatic binding and hydrophobic binding can be generated from one protein. For comparison to the models developed, sarcoplasmic reticulum Ca2 ion ATPase interaction with lipids will be measured by Raman spectroscopy to compare a real membrane system with the established models. This portion of the project will be a collabrative effort with Dr. P.L. Morse of the W.S.U. Biology Department. Dr. Morse has had extensive experience with SR Ca 2 ion ATPase.